The E.coli derived recombinant Biotin Labeled protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119, having an MW of 22kDa. The protein is fused to a beta-galactosidase (114 kDa) at the N-terminus.
The Hepatitis C Virus (HCV) is a significant global health concern, affecting millions of people worldwide. The virus primarily targets the liver, leading to chronic liver diseases such as cirrhosis and hepatocellular carcinoma. One of the key components of HCV is the core protein, which plays a crucial role in the virus’s life cycle and pathogenesis. The recombinant form of this core protein, conjugated with biotin, is widely used in research and diagnostic applications.
The core protein of HCV is a structural protein that forms the viral nucleocapsid. It is encoded by the 5’ end of the HCV genome and is approximately 21-23 kDa in size. The core protein is highly conserved among different HCV genotypes, making it an ideal target for diagnostic assays and vaccine development.
The recombinant HCV core protein is typically expressed in Escherichia coli (E. coli) systems. This method allows for high-yield production and easy purification of the protein. The recombinant protein is often fused with a tag, such as biotin, to facilitate its detection and immobilization in various assays.
Biotin is a small molecule that binds with high affinity to streptavidin and avidin, proteins commonly used in biochemical assays. Conjugating biotin to the HCV core protein enables its use in a variety of applications, including enzyme-linked immunosorbent assays (ELISA), western blotting (WB), and other immunoassays. The biotinylated core protein can be easily captured and detected using streptavidin-coated surfaces or beads.